摘要
应用荧光光谱(FS)和紫外光谱(UV)研究了尼莫地平与牛血清白蛋白(BSA)之间的相互作用。尼莫地平与BSA的结合常数KA为5.01×104(26℃)和4.46×104(36℃),尼莫地平在BSA上的结合位点数为1.08±0.01。根据Frster非辐射能量转移理论,求出了尼莫地平与BSA之间的结合距离为3.14nm(26℃)和3.10nm(36℃)。实验表明静态猝灭和非辐射能量转移是导致尼莫地平对BSA荧光猝灭的两大原因。通过计算热力学参数,可知该药物与牛血清白蛋白的相互作用是一个吉布斯自由能降低的自发过程,且二者之间的作用力以静电相互作用为主。
t The interaction of Nimodipine and bovine serum albumin （BSA） was studied using fluorescence spectroscopy （FS） and ultraviolet spectroscopy （UV）. The apparent binding constants （KA） between Nimodipine and BSA were 5. 01 ×10^4（26℃） and 4. 46×10^4（36℃）, and the binding sites （n） were 1.08±0.01. According to the Forster theory of non-radiation energy transfer, the binding distances （r） were also obtained. The experimental results showed that Nimodipine could quench the inner fluorescence of BSA by forming the Nimodipine-BSA complex. It was found that both static quenching and non-radiation energy transfer led to the fluorescence quenching. The process of binding was a spontaneous molecular interaction in which entropy increased while Gibbs free energy decreased. The thermodynamic parameters indicated that the interaction of Nimodipoine and BSA was driven mainly by static electrical force.
出处
《光谱学与光谱分析》
SCIE
EI
CAS
CSCD
北大核心
2007年第11期2317-2320,共4页
Spectroscopy and Spectral Analysis
基金
人事部留学人员科技择优项目
河北省自然科学基金项目(B2006000413)
河北农业大学科研发展基金项目资助
关键词
荧光光谱法
尼莫地平
牛血清白蛋白
相互作用
Fluorescence spectroscopy
Nimodipine
Bovine serum albttmin~ Interaction
